Mechanizm of an unique degrading behavior of bivalve molluscan collagen by protease digestion

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To elucidate the mechanism of an unique degrading behavior of bivalve molluscan collagen by protease digestion, the major twoα chains, named a and bchains, were isolated from the intact collagen preparation, prior to protease digestion, from scallop mantle, and their biochemical properties were investigated. Moreover, pepsin-solubilized collagen was found to have unusual solubility for collagens, showing high solubility around weak-basic pH. Based on this solubility, the major molecular species of collagen was successfully purified from pepsin-solubilized collagen preparation. It is necessary to identify the criticalα component for the unique degrading behavior by chasing the behavior of each majorα component on protease digestion.